Copper-binding motifs Xxx-His or Xxx-Zzz-His (ATCUN) linked to an antimicrobial peptide: Cu-binding, antimicrobial activity and ROS production.
Antimicrobial peptide
Copper
Metallopeptide
N-terminal Cu(II) binding site
Reactive oxygen species
Redox
Journal
Journal of inorganic biochemistry
ISSN: 1873-3344
Titre abrégé: J Inorg Biochem
Pays: United States
ID NLM: 7905788
Informations de publication
Date de publication:
12 2020
12 2020
Historique:
received:
19
05
2020
revised:
28
08
2020
accepted:
06
09
2020
pubmed:
28
9
2020
medline:
13
7
2021
entrez:
27
9
2020
Statut:
ppublish
Résumé
Depending on the coordination, copper ions can have a very high activity in catalyzing the production of reactive oxygen species. Thus interest arose in increasing the activity of antimicrobial peptides (AMPs) by equipping them with a Cu-binding unit. Several examples, native and engineered, have been investigated with the motif Xxx-Zzz-His, called Amino Terminal Cu(II)- and Ni(II)-binding (ATCUN) motif. Here we investigate a short AMP that was equipped either with Xxx-Zzz-His or Xxx-His. Xxx-His is a shorter motif and yields a more redox active copper complex. The control AMP, Xxx-His-AMP and Xxx-Zzz-His-AMP were investigated toward Cu-binding, Reactive Oxygen Species (ROS) production and antimicrobial activity in E. coli. The data indicate that these Cu-binding motifs have very limited impact on antimicrobial activity and low ROS production capability.
Identifiants
pubmed: 32980641
pii: S0162-0134(20)30283-X
doi: 10.1016/j.jinorgbio.2020.111255
pii:
doi:
Substances chimiques
Amino Acids
0
Pore Forming Cytotoxic Proteins
0
Reactive Oxygen Species
0
Copper
789U1901C5
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
111255Informations de copyright
Copyright © 2020 Elsevier Inc. All rights reserved.